17885-24-4

Basic information

• Product Name: 3-(ethyldisulfanyl)alanine
• CAS NO: 17885-24-4
• Molecular Formula: C₅H₁₁NO₂S₂
• Molecular Weight: 181.2763
• Mol File: 17885-24-4.mol
• Article Data: 6

Chemical Properties

• Boiling Point: 313.4°C at 760 mmHg
• Flash Point: 143.3°C
• Density: 1.316g/cm³
• Vapor Pressure: 0.000108mmHg at 25°C
• Refractive Index: 1.586
• CAS DataBase Reference: 3-(ethyldisulfanyl)alanine(CAS DataBase Reference)
• NIST Chemistry Reference: 3-(ethyldisulfanyl)alanine(17885-24-4)
• EPA Substance Registry System: 3-(ethyldisulfanyl)alanine(17885-24-4)

Safety Data

• Hazardous Substances Data: 17885-24-4(Hazardous Substances Data)

Usage

General Description

3-(ethyldisulfanyl)alanine is a chemical compound that consists of an alanine molecule with a disulfide group attached to the ethyl side chain. It is a nonpolar amino acid, and its structure allows it to participate in disulfide bond formation, which is important for the stability of proteins. 3-(ethyldisulfanyl)alanine is commonly found in proteins and plays a role in their structure and function. Its presence in the body can also have implications for certain disease states, as disulfide bond formation is relevant in oxidative stress and diseases related to protein misfolding. Overall, 3-(ethyldisulfanyl)alanine is an important chemical compound with significant biological relevance.

Upstream product

• 921-01-7 D-cysteine 
• 1208093-44-0 5,5-dimethyl-2-thiono-1,3,2-dioxaphosphorinanyl-2-disulfanylethane 
• 32443-99-5 D-cysteine hydrochloride 
• 75-08-1 ethanethiol 
• 59006-13-2 S-Guanylthio-cystein-dihydrochlorid 
• 18542-39-7 ethyl ethanethiosulfinate 
• 52-89-1 l-cysteine hydrochloride 
• 52-90-4 L-Cysteine 
• 1127-31-7 S-ethyl benzenethiosulfonate 
• 110-81-6 Diethyl disulfide 

Downstream Products

• 17885-30-2 ((R)-2-Benzyloxycarbonylamino-3-ethyldisulfanyl-propionylamino)-acetic acid ethyl ester 
• 76969-32-9 N-2,4-Dinitrophenyl-S-ethylthio-cystein 
• 110-81-6 Diethyl disulfide 
• 162377-46-0 N-Acetyl-S-(ethylsulfanyl)cysteine benzyl ester 
• 76969-35-2 p-Nitro-benzyloxycarbonyl-S-ethylthio-cystein-dicyclohexylammoniumsalz 
• 75305-87-2 N-2-Phenyl-iso-propyloxycarbonyl-S-ethylthio-cystein-dicyclohexylammoniumsalz 
• 75305-85-0 N-2-(p-Biphenylyl)-iso-propyloxycarbonyl-S-ethylthio-cystein-dicyclohexylammoniumsalz 
• 75305-96-3 N-2-Phenyl-iso-propyloxycarbonyl-S-ethylthio-cysteinyl-alanyl-leucin-tert.-butylester 

Relevant articles and documents

S-Alk(en)ylmercaptocysteine: Chemical synthesis, biological activities, and redox-related mechanism

S-Alk(en)ylmercaptocysteine (CySSR, R = methyl, ethyl, propyl, 1-propenyl, and allyl), which are the putative metabolites of Allium thiosulfinates, were chemically synthesized. CySSR, but not the corresponding monosulfide species S-alk(en)yl cysteine (CyS

A tissue homogenate method to prepare gram-scale allium thiosulfinates and their disulfide conjugates with cysteine and glutathione

The health benefits of Allium vegetables are widely attributed to the enzyme-derived organosulfur compounds called thiosulfinates (TS). However, the lack of a suitable method to prepare TS in good yields has hampered the evaluation of their biological activities. This paper describe a simple enzymatic method using Allium tissue homogenates as a reaction system to prepare gram-scale TS, including those enriched in 1-propenyl groups, which are particularly difficult to obtain. This method is simple, easy to scale up, and requires no column purification step, making it suitable for practical large-scale production of Allium TS. The prepared TS were further utilized to prepare the disulfide conjugates with cysteine and glutathione (CySSR and GSSR, R = methyl, ethyl, propyl, 1-propenyl, and allyl), which are the presumptive metabolites of TS. Among all of the Allium CySSR and GSSR conjugates, the newly prepared glutathione conjugate with 1-propenyl TS, GSSPe, showed the most potent effect to induce quinone reductase (QR, a representative phase II enzyme) in murine hepatoma cells (Hepa 1c1c7) and inhibit nitric oxide (NO) production in lipopolysaccharide (LPS)-stimulated macrophage cells (RAW 264.7).

Selectively S-Protected Cysteine Peptides. IV. Synthesis of Cysteine Peptides Using the S-Ethylthio Protecting Group. II

Studying the problems of the selective sulphur protection in cysteine peptides, a model octapeptide from the sheep insulin A-chain was prepared by conventional synthesis using the S-ethylthio and the S-diphenylmethyl group.As consequence of the small acid